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ACS Chem Biol. 2014 Jan 17;9(1):116-21. doi: 10.1021/cb400603t. Epub 2013 Nov 1.

Transmembrane type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity.

Author information

1
Division of Chemistry and Chemical Engineering and ‡Howard Hughes Medical Institute, California Institute of Technology , Pasadena, California 91125, United States of America.

Abstract

Metal selectivity in P1B-type ATPase transporters is determined by conserved amino acid residues in their transmembrane helices responsible for metal binding and transport across the cellular membrane. The Cu(2+)-selective CopB from Archaeoglobus fulgidus has been investigated to explore the coordination chemistry of the transition metal binding sites in P1B-3-type ATPases. Electronic absorption, electron paramagnetic resonance, and X-ray absorption spectroscopic studies indicate the presence of a high-affinity transmembrane Type-2-like Cu(2+) center in which a single cupric ion is coordinated in a distorted square pyramidal geometry by mixed nitrogen/oxygen and sulfur ligands.

PMID:
24144006
PMCID:
PMC3947036
DOI:
10.1021/cb400603t
[Indexed for MEDLINE]
Free PMC Article

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